Sandbox16

Protein: human Beta secretase complexed with inhibitor (1tqf)
By Amit Shavit and Nikola Finneran

Protein
A small molecule nonpeptide inhibitor of beta-secretase has been developed, and its binding has been defined through crystallographic determination of the enzyme-inhibitor complex. The molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the field of aspartyl protease inhibition. Additionally, the complex reveals a heretofore unknown S(3) subpocket that is created by the inhibitor. This structure has served an important role in the design of newer beta-secretase inhibitors. (http://www.proteopedia.org/wiki/index.php/1tqf)

Structure
Our protein is mostly composed of alpha helices (shown in red) and beta sheets (shown in blue) which contain some of the hydrophobic regions (shown in purple). The ligand in the center is highlighted in yellow.